ID   PIP_NEIGO               Reviewed;         310 AA.
AC   P42786;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Proline iminopeptidase;
DE            Short=PIP;
DE            EC=3.4.11.5;
DE   AltName: Full=Prolyl aminopeptidase;
DE            Short=PAP;
GN   Name=pip;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC   STRAIN=MS11 / MSO1-1X;
RX   PubMed=7934933; DOI=10.1111/j.1365-2958.1993.tb01249.x;
RA   Albertson N.H., Koomey M.;
RT   "Molecular cloning and characterization of a proline iminopeptidase gene
RT   from Neisseria gonorrhoeae.";
RL   Mol. Microbiol. 9:1203-1211(1993).
CC   -!- FUNCTION: Hydrolyzes peptides having the structure Pro-Y-Z to yield
CC       free proline. Also hydrolyzes the dipeptide Pro-Gly.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; Z25461; CAA80948.1; -; Genomic_DNA.
DR   PIR; S39592; S39592.
DR   RefSeq; WP_003688351.1; NZ_WHPL01000002.1.
DR   AlphaFoldDB; P42786; -.
DR   SMR; P42786; -.
DR   ESTHER; neigo-pip; Proline_iminopeptidase.
DR   MEROPS; S33.001; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR002410; Peptidase_S33.
DR   InterPro; IPR005944; Pro_iminopeptidase.
DR   PANTHER; PTHR43722; PTHR43722; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF006431; Pept_S33; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00793; PROAMNOPTASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   TIGRFAMs; TIGR01249; pro_imino_pep_1; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase; Protease.
FT   CHAIN           1..310
FT                   /note="Proline iminopeptidase"
FT                   /id="PRO_0000080841"
FT   DOMAIN          33..290
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        107
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        260
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        287
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34792 MW;  D0E7AEBA908A1AE0 CRC64;
     MYEIKQPFHS GYLQVSEIHQ IYWEESGNPD GVPVIFLHGG PGAGASPECR GFFNPDVFRI
     VIIDQRGCGR SHPYACAEDN TTWDLVADIE KVREMLGIGK WLVFGGSWGS TLSLAYAQTH
     PERVKGLVLR GIFLCRPSET AWLNEAGGVS RIYPEQWQKF VAPIAENRRN RLIEAYHGLL
     FHQDEEVCLS AAKAWADWES YLIRFEPEGV DEDAYASLAI ARLENHYFVN GGWLQGDKAI
     LNNIGKIRHI PTVIVQGRYD LCTPMQSAWE LSKAFPEAEL RVVQAGHCAF DPPLADALVQ
     AVEDILPRLL